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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
2 S-adenosyl-L-methionine + adenine2085 in a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA can be utilized efficiently as a substrate for methylation at adenine2085
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in a 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
the A2086T change is methylated to ca. 50% of the level of wild-type domain V
-
-
?
S-adenosyl-L-methionine + 23S rRNA
S-adenosyl-L-homocysteine + 23S rRNA containing N6-dimethyladenine
-
-
-
?
S-adenosyl-L-methionine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
S-adenosyl-L-homocysteine + 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
-
-
-
?
S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA containing N6-dimethyladenine
-
-
-
?
S-adenosyl-L-methionine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
S-adenosyl-L-homocysteine + 623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T containing N6-dimethyladenine
-
-
-
?
S-adenosyl-L-methionine + adenine2085 in 23S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
adenine2085 in 23S rRNA from Bacillus subtilis equals adenine2058 in Escherichia coli 23S rRNA
-
-
?
additional information
?
-
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis)
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
the rRNA methyltransferase ErmC0 transfers methyl groups from S-adenosyl-L-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ermC methyltransferase produces both N6-mono and N6,N6-dimethylated adenine residues in Bacillus subtilis 23 S rRNA during the course of the reaction in vitro. The addition of the two methyl groups to each 23 S rRNA molecule takes place through a monomethylated intermediate and suggest that the enzyme dissociates from its RNA substrate between the two consecutive methylation reactions. The enzyme is able to utilize monomethylated RNA as substrate for the addition of a second methyl group with an efficiency approximately comparable to that obtained when unmethylated RNA is the initial substrate
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
since methyl groups are incorporated in protein-free 23S rRNA molecules, the structure of rRNA alone must contain sufficient information to specify the methylation site. Highest incorporation is obtained with Bacillus subtilis 23S rRNA. Escherichia coli 23S rRNA acts as a poorer substrate (35% of the methylation obtained with Bacillus subtilis 23S rRNA)
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
synthetic 32-nt RNA oligonucleotide (5-GCGACGGACGGA2085AAGACCCCUAUCCGUCGCG-3, hairpin structure) designed to mimic the adenine loop in domain V of Bacillus subtilis 23S rRNA (residues 20732090 and 26382651)
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
the specificity of methylation on adenine2085 is confirmed by site-directed mutagenesis. All three mutated domain V fragments, A2085T, A2085G, and A2085C, are methylated to less than 10% of the level observed with the correct domain V RNA fragment. The G2084A change reduces the methylation of the resultant domain V fragment to ca. 12% of the level of the wild-type domain V fragment
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ermC methyltransferase produces both N6-mono and N6,N6-dimethylated adenine residues in Bacillus subtilis 23 S rRNA during the course of the reaction in vitro. The addition of the two methyl groups to each 23 S rRNA molecule takes place through a monomethylated intermediate and suggest that the enzyme dissociates from its RNA substrate between the two consecutive methylation reactions. The enzyme is able to utilize monomethylated RNA as substrate for the addition of a second methyl group with an efficiency approximately comparable to that obtained when unmethylated RNA is the initial substrate
-
-
?
additional information
?
-
direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
-
-
?
additional information
?
-
-
direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
S-adenosyl-L-methionine + adenine2085 in 23S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
adenine2085 in 23S rRNA from Bacillus subtilis equals adenine2058 in Escherichia coli 23S rRNA
-
-
?
additional information
?
-
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A2085 in Bacillus subtilis)
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
the rRNA methyltransferase ErmC0 transfers methyl groups from S-adenosyl-L-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics
-
-
?
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
-
-
-
?
additional information
?
-
direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
-
-
?
additional information
?
-
-
direct autoregulatory mechanism operating at the posttranscriptional level and independently of the ermC methylase-mediated methylation of ribosomes. A translational repression model is suggested in which the ermC methyltransferase binds to its own mRNA, at a region that resembles the methylation target site on 23S rRNA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-([[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl][3-(1H-imidazol-1-yl)propyl]amino]methyl)-1H-isoindole-1,3(2H)-dione
i.e. PD00556
4-methyl-2,6-di[(4-methylphenyl)thio]nicotinonitrile
i.e. RF00667
N6-dimethyladenine2085 containing 23S rRNA
linear competitive inhibition kinetics with RNA as the variable substrate, mixed inhibition with S-adenosyl-L-methionine as the variable substrate
-
nicotinaldehyde-N-[3-(2-chlorobenzyl)-3H-[1,2,3]triazolo[4,5-d]pyrimidin-7-yl]hydrazone
i.e. HTS12610
S-adenosyl-L-homocysteine
additional information
the crystal structure of ErmC methyltransferase is used as a target for structure-based virtual screening of a database composed of 58679 lead-like compounds. Among 77 compounds selected for experimental validation (63 predicted to bind to the catalytic pocket and 14 compounds predicted to bind to the putative RNA binding site), several novel inhibitors are found that decrease the minimal inhibitory concentration of a macrolide antibiotic erythromycin toward an Escherichia coli strain that constitutively expresses ErmC'. Analysis of docking models of the identified inhibitors suggests a novel strategy to develop potent and clinically useful inhibitors
-
S-adenosyl-L-homocysteine
linear competitive pattern with S-adenosyl-L-methionine as the variable substrate, and a mixed inhibition kinetics with RNA
S-adenosyl-L-homocysteine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000375
23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
0.00091
262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
0.0000344
623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
0.000144
623-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA with mutation A2086T
pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA
-
0.0003 - 0.012
adenine2085 in 23S rRNA
-
0.000354 - 0.0257
S-adenosyl-L-methionine
additional information
additional information
-
0.0003
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E128A
-
0.000375
adenine2085 in 23S rRNA
pH 7.5, 37°C
-
0.00043
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme T108A
-
0.00057
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E202A
-
0.00062
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme M196A
-
0.00069
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
0.0007
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
0.00079
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N192A
-
0.0008
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N101A
-
0.0008
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N11A
-
0.00089
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K204A
-
0.00089
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N200A
-
0.00091
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K205A
-
0.00095
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K209A
-
0.00121
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
-
0.0013
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme P165A
-
0.0014
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme F163A
-
0.0014
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K168A
-
0.00141
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R140A
-
0.00159
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A
-
0.0017
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112A
-
0.00186
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K133A
-
0.0025
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R134A
-
0.00364
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112D
-
0.0041
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K166A
-
0.012
adenine2085 in 23S rRNA
pH 7.5, 37°C
-
0.000354
S-adenosyl-L-methionine
pH 7.5, 37°C
0.002
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme F163A
0.002
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N192A
0.0028
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
0.003
S-adenosyl-L-methionine
pH 7.5, 21°C
0.003
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A
0.003
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme M196A
0.0031
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K166A
0.0038
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K204A
0.004
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K168A
0.004
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N11A
0.0044
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K205A
0.0045
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E128A
0.0046
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K209A
0.0058
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112A
0.006
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K133A
0.0066
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
0.007
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N200A
0.0098
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E202A
0.011
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112D
0.012
S-adenosyl-L-methionine
pH 7.5, 37°C
0.0139
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N101A
0.0185
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme P165A
0.021
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R134A
0.022
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R140A
0.0257
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme T108A
additional information
additional information
interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
-
additional information
additional information
-
interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00011 - 2.2
adenine2085 in 23S rRNA
-
0.0121 - 0.0775
S-adenosyl-L-methionine
additional information
additional information
-
0.00011
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme T108A
-
0.00021
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R134A
-
0.00034
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R140A
-
0.00049
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112D
-
0.00113
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112A
-
0.00193
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
-
0.00211
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E202A
-
0.00222
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K133A
-
0.00318
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme M196A
-
0.00439
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N200A
-
0.00544
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N192A
-
0.00637
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
0.00637
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K209A
-
0.00729
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K204A
-
0.00731
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A
-
0.00766
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K205A
-
0.04
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme P165A
-
0.07
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N101A
-
0.19
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E128A
-
0.23
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N11A
-
0.37
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme F163A
-
0.64
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
0.87
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K168A
-
2.2
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K166A
-
0.0121
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112D
0.0149
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R140A
0.0157
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R134A
0.016
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme P165A
0.0161
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112A
0.0229
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme T108A
0.029
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N11A
0.0314
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
0.0318
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme M196A
0.032
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme F163A
0.033
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N101A
0.0341
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N192A
0.038
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K133A
0.048
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E128A
0.0522
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A
0.054
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K166A
0.054
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K168A
0.0648
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K204A
0.0649
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K205A
0.0655
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
0.066
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
0.0688
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N200A
0.0735
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E202A
0.0775
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K209A
additional information
additional information
interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
-
additional information
additional information
-
interaction between 23s rRNA and ermC' methyltransferase. Kinetic and thermodynamic parameters of binding are determined
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.066 - 914
adenine2085 in 23S rRNA
-
0.67 - 23.6
S-adenosyl-L-methionine
0.066
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112A
-
0.084
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R134A
-
0.135
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R112D
-
0.241
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme R140A
-
0.258
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme T108A
-
1.193
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K133A
-
1.6
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
-
3.7
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E202A
-
4.6
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K197A
-
4.9
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N200A
-
5.13
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme M196A
-
6.71
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K209A
-
6.89
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N192A
-
8.19
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K204A
-
8.42
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K205A
-
9.23
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
30.7
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme P165A
-
87.5
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N101A
-
264
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme F163A
-
287.5
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme N11A
-
536
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K166A
-
621
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme K168A
-
633
adenine2085 in 23S rRNA
pH 7.5, 25°C, mutant enzyme E128A
-
914
adenine2085 in 23S rRNA
pH 7.5, 25°C, wild-type enzyme
-
0.67
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R140A
0.74
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R134A
0.86
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme P165A
0.89
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme T108A
1.12
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112D
1.47
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K205A
2.4
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N101A
2.78
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme R112A
4.79
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A
6.33
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K133A
7.3
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N11A
7.53
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E202A
9.64
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme M196A
9.7
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N200A
10.7
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme E128A
13.5
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K168A
15.63
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K197A
16
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme F163A
16.77
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K209A
16.92
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K204A
17.05
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme N192A
17.4
S-adenosyl-L-methionine
pH 7.5, 25°C, mutant enzyme K166A
23.23
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
23.6
S-adenosyl-L-methionine
pH 7.5, 25°C, wild-type enzyme
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E128A
kcat/KM for S-adenosyl-L-methionine is 46% of wild type value. kcat/KM for RNA is 59% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
E202A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 32% of the wild-type value. kcat/Km for RNA is 40% of wild-type value
F163A
kcat/KM for S-adenosyl-L-methionine is 67% of wild type value. kcat/KM for RNA is 28% of wild type value. Mutant enzyme still mediates erythromycin resistance, although at reduced level
K133A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. No change in affinity towards the RNA substrate. kcat/Km for S-adenosyl-L-methionine is% of the wild-type value. kcat/Km for RNA is 27% of wild-type value. kcat/Km for S-adenosyl-L-methionine is 13% of the wild-type value. kcat/Km for RNA is% of wild-type value
K166A
kcat/KM for S-adenosyl-L-methionine is 74% of wild type value. kcat/KM for RNA is 58% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
K168A
kcat/KM for S-adenosyl-L-methionine is 59% of wild type value. kcat/KM for RNA is 70% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
K197A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 67% of the wild-type value. kcat/Km for RNA is 50% of wild-type value
K197A/N200A/E202A/K204A/K205A
the five mutations together do not show a visible cumulative effect on the ErmC' activity in vivo
K204A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 73% of the wild-type value. kcat/Km for RNA is 89% of wild-type value
K205A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 63% of the wild-type value. kcat/Km for RNA is 92% of wild-type value
K209A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 72% of the wild-type value. kcat/Km for RNA is 73% of wild-type value
M196A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 42% of the wild-type value. kcat/Km for RNA is 56% of wild-type value
N101A
kcat/KM for S-adenosyl-L-methionine is 10% of wild type value. kcat/KM for RNA is 11% of wild type value. Mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
N11A
kcat/KM for S-adenosyl-L-methionine is 32% of wild type value. kcat/KM for RNA is 33% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
N192A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 73% of the wild-type value. kcat/Km for RNA is 74% of wild-type value
N200A
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 42% of the wild-type value. kcat/Km for RNA is 54% of wild-type value
P165A
kcat/KM for S-adenosyl-L-methionine is 4% of wild type value. kcat/KM for RNA is 4% of wild type value. Mutant enzyme still mediates erythromycin resistance, although at reduced level
R112A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 12% of the wild-type value. kcat/Km for RNA is 7% of wild-type value
R112D
decreased ability in rendering DH5alpha cells resistant to erythromycin. The R112D mutant shows a more pronounced decrease in RNA-binding affinity compared with R112A. kcat/Km for S-adenosyl-L-methionine is 5% of the wild-type value. kcat/Km for RNA is 2% of wild-type value
R134A
mutant exhibits the most severe effect on the ErmC' ability to generate erythromycin resistance, this mutant has completely lost the activity in vivo. kcat/Km for S-adenosyl-L-methionine is 3% of the wild-type value. kcat/Km for RNA is 1% of wild-type value
R140A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 1% of the wild-type value. kcat/Km for RNA is 3% of wild-type value
T108A
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 4% of the wild-type value. kcat/Km for RNA is 3% of wild-type value
Y104A
mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
E128A
-
kcat/KM for S-adenosyl-L-methionine is 46% of wild type value. kcat/KM for RNA is 59% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
-
E202A
-
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 32% of the wild-type value. kcat/Km for RNA is 40% of wild-type value
-
K133A
-
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. No change in affinity towards the RNA substrate. kcat/Km for S-adenosyl-L-methionine is% of the wild-type value. kcat/Km for RNA is 27% of wild-type value. kcat/Km for S-adenosyl-L-methionine is 13% of the wild-type value. kcat/Km for RNA is% of wild-type value
-
K168A
-
kcat/KM for S-adenosyl-L-methionine is 59% of wild type value. kcat/KM for RNA is 70% of wild type value. No difference in generating erythromycin resistance when compared to the wild-type enzyme
-
K197A
-
mutant of a residues positioned on the surface of the small domain, does not display substantial defects in activity compared with the wild-type enzyme. kcat/Km for S-adenosyl-L-methionine is 67% of the wild-type value. kcat/Km for RNA is 50% of wild-type value
-
N11A
-
kcat/KM for S-adenosyl-L-methionine is 32% of wild type value. kcat/KM for RNA is 33% of wild type value. Little difference in generating erythromycin resistance when compared to the wild-type enzyme
-
R112A
-
decreased ability in rendering DH5alpha cells resistant to erythromycin, suggesting that this amino acid is not absolutely indispensable for the ErmC' activity, but might be involved in important RNA-protein interactions. kcat/Km for S-adenosyl-L-methionine is 12% of the wild-type value. kcat/Km for RNA is 7% of wild-type value
-
Y104A
-
mutant enzyme is totally unable to render DH5alpha cells resistant to erythromycin
-
additional information
to validate the structure-based predictions of presumably essential residues in the catalytic pocket of ErmC', site-directed mutagenesis is carried out and the function of the mutants is studied in vitro and in vivo
additional information
With the aim of identification of essential protein-RNA interactions, charged side chains on the predicted target-binding surface of ErmC' are replaced systematically with alanine and the function of the single- and multiple-site mutants is studied in vitro and in vivo. kcat/Km for S-adenosyl-L-methionine is 21% of the wild-type value. kcat/Km for RNA is 17% of wild-type value
additional information
-
to validate the structure-based predictions of presumably essential residues in the catalytic pocket of ErmC', site-directed mutagenesis is carried out and the function of the mutants is studied in vitro and in vivo
-
additional information
-
With the aim of identification of essential protein-RNA interactions, charged side chains on the predicted target-binding surface of ErmC' are replaced systematically with alanine and the function of the single- and multiple-site mutants is studied in vitro and in vivo. kcat/Km for S-adenosyl-L-methionine is 21% of the wild-type value. kcat/Km for RNA is 17% of wild-type value
-
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Denoya, C.; Dubnau, D.
Site and substrate specificity of the ermC 23S rRNA methyltransferase
J. Bacteriol.
169
3857-3860
1987
Bacillus subtilis (P13956), Bacillus subtilis
brenda
Denoya, C.; Dubnau, D.
Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase
J. Biol. Chem.
264
2615-2624
1989
Bacillus subtilis (P13956), Bacillus subtilis BD170 (P13956)
brenda
Bussiere, D.E.; Muchmore, S.W.; Dealwis, C.G.; Schluckebier, G.; Nienaber, V.L.; Edalji, R.P.; Walter, K.A.; Ladror, U.S.; Holzman, T.F.; Abad-Zapatero, C.
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria
Biochemistry
37
7103-7112
1998
Bacillus subtilis (P13956), Bacillus subtilis
brenda
Maravic, G.; Feder, M.; Pongor, S.; Flogel, M.; Bujnicki, J.M.
Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC'
J. Mol. Biol.
332
99-109
2003
Bacillus subtilis (P13956), Bacillus subtilis BD1167 (P13956)
brenda
Su, S.L.
Dubnau, D.: Binding of Bacillus subtilis ermC' methyltransferase to 23S rRNA
Biochemistry
29
6033-6042
1990
Bacillus subtilis (P13956), Bacillus subtilis
brenda
Feder, M.; Purta, E.; Koscinski, L.; Ebrilo, S.; Vlahovicek, G.; Bujnicki, J.
Virtual screening and experimental verification to identify potential inhibitors of the ErmC methyltransferase responsible for bacterial resistance against macrolide antibiotics
ChemMedChem
3
316-322
2008
Bacillus subtilis (P13956)
brenda
Denoya, C.D.; Bechhofer, D.H.; Dubnau, D.
Translational autoregulation of ermC 23S rRNA methyltransferase expression in Bacillus subtilis
J. Bacteriol.
168
1133-1141
1986
Bacillus subtilis (P13956), Bacillus subtilis
brenda
Kadam, S.K.
Induction of ermC methylase in the absence of macrolide antibiotics and by pseudomonic acid A
J. Bacteriol.
171
4518-4520
1989
Bacillus subtilis (P13956)
brenda
Zhong, P.; Pratt, S.D.; Edalji, R.P.; Walter, K.A.; Holzman, T.F.; Shivakumar, A.G.; Katz, L.
Substrate requirements for ErmC' methyltransferase activity
J. Bacteriol.
177
4327-4332
1995
Bacillus subtilis (P13956), Bacillus subtilis
brenda
Schluckebier, G.; Zhong, P.; Stewart, K.D.
Kavanaugh, T.J.; Abad-Zapatero, C.: The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism
J. Mol. Biol.
289
277-291
1999
Bacillus subtilis (P13956)
brenda
Maravic, G.; Bujnicki, J.M.; Feder, M.; Pongor, S.; Flgel, M.
Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions
Nucleic Acids Res.
31
4941-4949
2003
Bacillus subtilis (P13956), Bacillus subtilis BD1167 (P13956)
brenda
Gul, N.; Linares, D.M.; Ho, F.Y.; Poolman, B.
Evolved Escherichia coli strains for amplified, functional expression of membrane proteins
J. Mol. Biol.
426
136-149
2014
Escherichia coli
brenda